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Structure paper

TitleTrapping biosynthetic acyl-enzyme intermediates with encoded 2,3-diaminopropionic acid.
Journal, issue, pagesNature, Vol. 565, Page 112-117, Year 2019
Publish dateAug 7, 2018 (structure data deposition date)
AuthorsHuguenin-Dezot, N. / Alonzo, D.A. / Heberlig, G.W. / Mahesh, M. / Nguyen, D.P. / Dornan, M.H. / Boddy, C.N. / Schmeing, T.M. / Chin, J.W.
External linksNature / PubMed:30542153
MethodsX-ray diffraction
Resolution1.7 - 2.5 Å
Structure data

PDB-6ecb:
Vlm2 thioesterase domain wild type structure 1
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-6ecc:
Vlm2 thioesterase domain wild type structure 2
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-6ecd:
Vlm2 thioesterase domain with genetically encoded 2,3-diaminopropionic acid bound with a tetradepsipeptide
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-6ece:
Vlm2 thioesterase domain with genetically encoded 2,3-diaminopropionic acid bound with a dodecadepsipeptide, space group H3
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-6ecf:
Vlm2 thioesterase domain with genetically encoded 2,3-diaminopropionic acid bound with a dodecadepsipeptide, space group P1
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • streptomyces tsusimaensis (bacteria)
  • synthetic construct (others)
KeywordsHYDROLASE / thioesterase / thioesterase domain / NRPS / non-ribosomal peptide synthetase / nonribosomal peptide synthetase / valinomycin / depsipeptide / unnatural amino acid / 2 / 3-diaminopropionic acid

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